Distinct inactive conformations of the dopamine D2 and D3 receptors correspond to different extents of inverse agonism

By analyzing and simulating inactive conformations of the highly homologous dopamine D(2) and D(3) receptors (D(2)R and D(3)R), we find that eticlopride binds D(2)R in a pose very similar to that in the D(3)R/eticlopride structure but incompatible with the D(2)R/risperidone structure. In addition, r...

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Detalles Bibliográficos
Autores principales: Lane, J Robert, Abramyan, Ara M, Adhikari, Pramisha, Keen, Alastair C, Lee, Kuo-Hao, Sanchez, Julie, Verma, Ravi Kumar, Lim, Herman D, Yano, Hideaki, Javitch, Jonathan A, Shi, Lei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2020
Materias:
Biochemistry and Chemical Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7053997/
https://www.ncbi.nlm.nih.gov/pubmed/31985399
http://dx.doi.org/10.7554/eLife.52189

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7053997/
https://www.ncbi.nlm.nih.gov/pubmed/31985399
http://dx.doi.org/10.7554/eLife.52189

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